Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Karen J. Martell"'
Publikováno v:
Journal of Biological Chemistry. 269:3596-3604
Vaccinia phosphatase VH-1 and its mammalian counterparts, including protein-tyrosine phosphatases (PTPase) CL100 and VHR, constitute a novel subfamily of protein-tyrosine phosphatases that exhibits dual substrate specificity for phosphotyrosine- and
Publikováno v:
Neuron. 11:387-400
Tyrosine phosphorylation plays a central role in the control of neuronal cell development and function. Yet, few neuronal protein tyrosine phosphatases (PTPs) have been identified. We examined rat olfactory neuroepithelium for expression of novel PTP
Autor:
Karen J. Martell, Jack E. Dixon, David Hakes, Joseph J. Esposito, Robert F. Massung, Wei-Guo Zhao
Publikováno v:
Proceedings of the National Academy of Sciences. 90:4017-4021
The vaccinia virus VH1 gene product is a dual specificity protein phosphatase with activity against both phosphoserine- and phosphotyrosine-containing substrates. We investigated the potential presence of VH1 analogs in other viruses. Hybridization a
Publikováno v:
Pharmacogenetics. 3:71-76
The increased risk of rapid acetylator humans for the development of colorectal cancer has created interest in experimental animal models to study the relationship of N-acetyltransferase phenotype to colon cancer. Colon cytosols from inbred mouse lin
Publikováno v:
Pharmacogenetics. 2:197-206
Over the past 10 years, much fascinating information has been obtained concerning the biochemistry, genetics, toxicological implications and molecular genetics of the N-acetylation polymorphism in mice. Using C57BL/6J (B6) mice as representative of r
Publikováno v:
Journal of Biological Chemistry. 265:4863-4870
Cytosols contain a heat-stable, chelatable, anionic, molybdate-like factor that stabilizes glucocorticoid receptors in a heteromeric complex with hsp90 (refers to the 90-kDa heat shock protein) and inhibits their transformation to the DNA-binding sta
Publikováno v:
Genomics. 22:462-464
Four human protein-tyrosine phosphatase (PTPase) genes of the VH1-like subclass were cloned by low-stringency screening of a genomic library. These genes were localized to their respective chromosomes by G-banding and fluorescence in situ hybridizati
Publikováno v:
Journal of neurochemistry. 65(4)
A novel protein tyrosine phosphatase [homologue of vaccinia virus H1 phosphatase gene clone 5 (hVH-5)] was cloned; it shared sequence similarity with a subset of protein tyrosine phosphatases that regulate mitogen-activated protein kinase. The cataly
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 88(14)
Classification of humans as rapid or slow acetylators is based on hereditary differences in rates of N-acetylation of therapeutic and carcinogenic agents, but N-acetylation of certain arylamine drugs displays no genetic variations. Two highly homolog